ID   ACYP2_MELGA             Reviewed;         103 AA.
AC   P00821;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   25-MAY-2022, entry version 104.
DE   RecName: Full=Acylphosphatase-2;
DE            EC=3.6.1.7;
DE   AltName: Full=Acylphosphatase isozyme TU1;
DE   AltName: Full=Acylphosphatase, muscle type isozyme;
DE   AltName: Full=Acylphosphate phosphohydrolase 2;
GN   Name=ACYP2;
OS   Meleagris gallopavo (Wild turkey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Meleagridinae; Meleagris.
OX   NCBI_TaxID=9103;
RN   [1]
RP   PROTEIN SEQUENCE OF 2-103, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT
RP   SER-2, AND GLUTATHIONYLATION AT CYS-26.
RC   TISSUE=Skeletal muscle;
RX   PubMed=6317387; DOI=10.1111/j.1432-1033.1983.tb07825.x;
RA   Camici G., Manao G., Cappugi G., Berti A., Stefani M., Liguri G.,
RA   Ramponi G.;
RT   "The primary structure of turkey muscle acylphosphatase.";
RL   Eur. J. Biochem. 137:269-277(1983).
CC   -!- FUNCTION: Its physiological role is not yet clear.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=an acyl phosphate + H2O = a carboxylate + H(+) + phosphate;
CC         Xref=Rhea:RHEA:14965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:29067, ChEBI:CHEBI:43474, ChEBI:CHEBI:59918; EC=3.6.1.7;
CC   -!- SUBUNIT: Monomer (TU1) or homodimer (TU3) in absence of reducing
CC       factors; disulfide linked.
CC   -!- SIMILARITY: Belongs to the acylphosphatase family. {ECO:0000305}.
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DR   PIR; A01018; QPTK.
DR   AlphaFoldDB; P00821; -.
DR   SMR; P00821; -.
DR   iPTMnet; P00821; -.
DR   InParanoid; P00821; -.
DR   Proteomes; UP000001645; Unplaced.
DR   GO; GO:0003998; F:acylphosphatase activity; IEA:UniProtKB-EC.
DR   InterPro; IPR020456; Acylphosphatase.
DR   InterPro; IPR001792; Acylphosphatase-like_dom.
DR   InterPro; IPR036046; Acylphosphatase-like_dom_sf.
DR   InterPro; IPR017968; Acylphosphatase_CS.
DR   PANTHER; PTHR10029; PTHR10029; 1.
DR   Pfam; PF00708; Acylphosphatase; 1.
DR   PRINTS; PR00112; ACYLPHPHTASE.
DR   SUPFAM; SSF54975; SSF54975; 1.
DR   PROSITE; PS00150; ACYLPHOSPHATASE_1; 1.
DR   PROSITE; PS00151; ACYLPHOSPHATASE_2; 1.
DR   PROSITE; PS51160; ACYLPHOSPHATASE_3; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Direct protein sequencing; Disulfide bond; Glutathionylation;
KW   Hydrolase; Reference proteome.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250"
FT   CHAIN           2..103
FT                   /note="Acylphosphatase-2"
FT                   /id="PRO_0000158549"
FT   DOMAIN          13..103
FT                   /note="Acylphosphatase-like"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00520"
FT   ACT_SITE        28
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00520"
FT   ACT_SITE        46
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00520"
FT   MOD_RES         2
FT                   /note="N-acetylserine"
FT                   /evidence="ECO:0000269|PubMed:6317387"
FT   MOD_RES         26
FT                   /note="S-glutathionyl cysteine; alternate"
FT                   /evidence="ECO:0000269|PubMed:6317387"
FT   DISULFID        26
FT                   /note="Interchain; alternate"
SQ   SEQUENCE   103 AA;  11448 MW;  23D12EB987EC37C8 CRC64;
     MSALTKASGA LKSVDYEVFG RVQGVCFRMY TEEEARKLGV VGWVKNTRQG TVTGQVQGPE
     DKVNAMKSWL SKVGSPSSRI DRTNFSNEKE ISKLDFSGFS TRY